An odorant receptor tuned to an attractive plant volatile vanillin in Spodoptera litura.

Molecular docking Oviposition preference The common cutworm Two-electrode voltage clamp recording Xenopus oocyte Y-tube olfactometer

Journal

Pesticide biochemistry and physiology
ISSN: 1095-9939
Titre abrégé: Pestic Biochem Physiol
Pays: United States
ID NLM: 1301573

Informations de publication

Date de publication:
Nov 2023
Historique:
received: 11 08 2023
revised: 02 09 2023
accepted: 11 09 2023
medline: 13 11 2023
pubmed: 10 11 2023
entrez: 9 11 2023
Statut: ppublish

Résumé

The insect olfaction plays crucial roles in many important behaviors, in which ORs are key determinants for signal transduction and the olfactory specificity. Spodoptera litura is a typical polyphagous pest, possessing a large repertoire of ORs tuning to broad range of plant odorants. However, the specific functions of those ORs remain mostly unknown. In this study, we functionally characterized one S. litura OR (OR51) that was highly expressed in the adult antennae. First, by using Xenopus oocyte expression and two-electrode voltage clamp recording system (XOE-TEVC), OR51 was found to be strongly and specifically responsive to vanillin (a volatile of S. litura host plants) among 77 tested odorants. Second, electroantennogram (EAG) and Y-tube behavioral experiment showed that vanillin elicited significant EAG response and attraction behavior especially of female adults. This female attraction was further confirmed by the oviposition experiment, in which the soybean plants treated with vanillin were significantly preferred by females for egg-laying. Third, 3D structural modelling and molecular docking were conducted to explore the interaction between OR51 and vanillin, which showed a high affinity (-4.46 kcal/mol) and three residues (Gln163, Phe164 and Ala305) forming hydrogen bonds with vanillin, supporting the specific binding of OR51 to vanillin. In addition, OR51 and its homologs from other seven noctuid species shared high amino acid identities (78-97%) and the same three hydrogen bond forming residues, suggesting a conserved function of the OR in these insects. Taken together, our study provides some new insights into the olfactory mechanisms of host plant finding and suggests potential applications of vanillin in S. litura control.

Identifiants

pubmed: 37945255
pii: S0048-3575(23)00284-5
doi: 10.1016/j.pestbp.2023.105619
pii:
doi:

Substances chimiques

Receptors, Odorant 0
vanillin CHI530446X
Insect Proteins 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

105619

Informations de copyright

Copyright © 2023 Elsevier Inc. All rights reserved.

Auteurs

Zhi-Qiang Wei (ZQ)

Key Laboratory of Integrated Management of Crop Disease and Pests, Ministry of Education / College of Plant Protection, Nanjing Agricultural University, Nanjing 210095, China.

Ji-Xiang Wang (JX)

Key Laboratory of Integrated Management of Crop Disease and Pests, Ministry of Education / College of Plant Protection, Nanjing Agricultural University, Nanjing 210095, China.

Jin-Meng Guo (JM)

Key Laboratory of Integrated Management of Crop Disease and Pests, Ministry of Education / College of Plant Protection, Nanjing Agricultural University, Nanjing 210095, China.

Xiao-Long Liu (XL)

Key Laboratory of Integrated Management of Crop Disease and Pests, Ministry of Education / College of Plant Protection, Nanjing Agricultural University, Nanjing 210095, China.

Qi Yan (Q)

Key Laboratory of Integrated Management of Crop Disease and Pests, Ministry of Education / College of Plant Protection, Nanjing Agricultural University, Nanjing 210095, China.

Jin Zhang (J)

Key Laboratory of Integrated Management of Crop Disease and Pests, Ministry of Education / College of Plant Protection, Nanjing Agricultural University, Nanjing 210095, China.

Shuang-Lin Dong (SL)

Key Laboratory of Integrated Management of Crop Disease and Pests, Ministry of Education / College of Plant Protection, Nanjing Agricultural University, Nanjing 210095, China. Electronic address: sldong@njau.edu.cn.

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Classifications MeSH